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Protein

Isoaspartyl peptidase/L-asparaginase

Gene

Asrgl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Has both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine.By similarity

Catalytic activityi

L-asparagine + H2O = L-aspartate + NH3.By similarity
Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei185 – 1851NucleophileBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease

Enzyme and pathway databases

ReactomeiR-MMU-71182. Phenylalanine and tyrosine catabolism.

Protein family/group databases

MEROPSiT02.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Isoaspartyl peptidase/L-asparaginase (EC:3.4.19.5By similarity, EC:3.5.1.1By similarity)
Alternative name(s):
Asparaginase-like protein 1
Beta-aspartyl-peptidase
Isoaspartyl dipeptidase
L-asparagine amidohydrolase
Cleaved into the following 2 chains:
Gene namesi
Name:Asrgl1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1913764. Asrgl1.

Subcellular locationi

  • Cytoplasm By similarity

  • Note: Midpiece of sperm tail.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 184184Isoaspartyl peptidase/L-asparaginase alpha chainPRO_0000420559Add
BLAST
Chaini185 – 326142Isoaspartyl peptidase/L-asparaginase beta chainPRO_0000420560Add
BLAST

Post-translational modificationi

Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity.By similarity

Keywords - PTMi

Autocatalytic cleavage

Proteomic databases

EPDiQ8C0M9.
MaxQBiQ8C0M9.
PaxDbiQ8C0M9.
PeptideAtlasiQ8C0M9.
PRIDEiQ8C0M9.

2D gel databases

REPRODUCTION-2DPAGEIPI00223875.

PTM databases

PhosphoSiteiQ8C0M9.
SwissPalmiQ8C0M9.

Expressioni

Gene expression databases

BgeeiQ8C0M9.
CleanExiMM_ASRGL1.
GenevisibleiQ8C0M9. MM.

Interactioni

Subunit structurei

Heterodimer of an alpha and beta chain produced by autocleavage. This heterodimer may then dimerize in turn, giving rise to a heterotetramer.By similarity

Protein-protein interaction databases

BioGridi211529. 1 interaction.
IntActiQ8C0M9. 2 interactions.
MINTiMINT-4125411.
STRINGi10090.ENSMUSP00000051709.

Structurei

3D structure databases

ProteinModelPortaliQ8C0M9.
SMRiQ8C0M9. Positions 21-325.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni213 – 2164Substrate bindingBy similarity
Regioni236 – 2394Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the Ntn-hydrolase family.Curated

Phylogenomic databases

eggNOGiKOG1592. Eukaryota.
COG1446. LUCA.
GeneTreeiENSGT00530000063034.
HOGENOMiHOG000174613.
HOVERGENiHBG101662.
InParanoidiQ8C0M9.
KOiK13051.
OMAiPCVGAGG.
OrthoDBiEOG7TBC2N.
PhylomeDBiQ8C0M9.
TreeFamiTF323960.

Family and domain databases

InterProiIPR029055. Ntn_hydrolases_N.
IPR000246. Peptidase_T2.
[Graphical view]
PANTHERiPTHR10188. PTHR10188. 1 hit.
PfamiPF01112. Asparaginase_2. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8C0M9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MACARGTVAP PVRASIDVSL VVVVHGGGAS NISANRKELV REGIARAATE
60 70 80 90 100
GYKILKAGGS AVDAVEGAVT VLENDPEFNA GYGSVLNVNG DIEMDASIMD
110 120 130 140 150
GKDLSAGAVS AVRCIANPVK LARLVMEKTP HCFLTGHGAE KFAEDMGIPQ
160 170 180 190 200
VPVEKLITER TKKHLEKEKL EKGAQNADCP KNSGTVGAVA LDCRGNLAYA
210 220 230 240 250
TSTGGIVNKM VGRVGDSPCI GAGGYADNNL GAVSTTGHGE SILKVNLARL
260 270 280 290 300
ALFHVEQGKT VEEAAQLALD YMKSKLKGLG GLILVNKTGD WVAKWTSASM
310 320
PWAAVKNGKL QAGIDLCETR TRDLPC
Length:326
Mass (Da):33,950
Last modified:March 1, 2003 - v1
Checksum:iB5AC25922D9A1338
GO

Sequence cautioni

The sequence AAH16106.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB24431.1 differs from that shown. Reason: Frameshift at position 29. Curated
The sequence BAC25294.1 differs from that shown. Reason: Frameshift at positions 24 and 29. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK006147 mRNA. Translation: BAB24431.1. Frameshift.
AK010381 mRNA. Translation: BAC25294.1. Frameshift.
AK030209 mRNA. Translation: BAC26844.1.
BC016106 mRNA. Translation: AAH16106.1. Different initiation.
CCDSiCCDS29566.1.
RefSeqiNP_079886.2. NM_025610.3.
UniGeneiMm.272847.

Genome annotation databases

EnsembliENSMUST00000049948; ENSMUSP00000051709; ENSMUSG00000024654.
GeneIDi66514.
KEGGimmu:66514.
UCSCiuc008gon.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK006147 mRNA. Translation: BAB24431.1. Frameshift.
AK010381 mRNA. Translation: BAC25294.1. Frameshift.
AK030209 mRNA. Translation: BAC26844.1.
BC016106 mRNA. Translation: AAH16106.1. Different initiation.
CCDSiCCDS29566.1.
RefSeqiNP_079886.2. NM_025610.3.
UniGeneiMm.272847.

3D structure databases

ProteinModelPortaliQ8C0M9.
SMRiQ8C0M9. Positions 21-325.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211529. 1 interaction.
IntActiQ8C0M9. 2 interactions.
MINTiMINT-4125411.
STRINGi10090.ENSMUSP00000051709.

Protein family/group databases

MEROPSiT02.002.

PTM databases

PhosphoSiteiQ8C0M9.
SwissPalmiQ8C0M9.

2D gel databases

REPRODUCTION-2DPAGEIPI00223875.

Proteomic databases

EPDiQ8C0M9.
MaxQBiQ8C0M9.
PaxDbiQ8C0M9.
PeptideAtlasiQ8C0M9.
PRIDEiQ8C0M9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000049948; ENSMUSP00000051709; ENSMUSG00000024654.
GeneIDi66514.
KEGGimmu:66514.
UCSCiuc008gon.1. mouse.

Organism-specific databases

CTDi80150.
MGIiMGI:1913764. Asrgl1.

Phylogenomic databases

eggNOGiKOG1592. Eukaryota.
COG1446. LUCA.
GeneTreeiENSGT00530000063034.
HOGENOMiHOG000174613.
HOVERGENiHBG101662.
InParanoidiQ8C0M9.
KOiK13051.
OMAiPCVGAGG.
OrthoDBiEOG7TBC2N.
PhylomeDBiQ8C0M9.
TreeFamiTF323960.

Enzyme and pathway databases

ReactomeiR-MMU-71182. Phenylalanine and tyrosine catabolism.

Miscellaneous databases

ChiTaRSiAsrgl1. mouse.
PROiQ8C0M9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C0M9.
CleanExiMM_ASRGL1.
GenevisibleiQ8C0M9. MM.

Family and domain databases

InterProiIPR029055. Ntn_hydrolases_N.
IPR000246. Peptidase_T2.
[Graphical view]
PANTHERiPTHR10188. PTHR10188. 1 hit.
PfamiPF01112. Asparaginase_2. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Testis.
  2. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 6-13; 103-120 AND 129-155, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 80-326.
    Strain: FVB/N.
    Tissue: Salivary gland.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiASGL1_MOUSE
AccessioniPrimary (citable) accession number: Q8C0M9
Secondary accession number(s): Q91WC8, Q9CVX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.